Crystal structure of the C-terminal globular domain of the third paralog of the Archaeoglobus fulgidus oligosaccharyltransferases

Table 1 Data collection and refinement statistics

	Native	Se-SAD
Data collection statistics ^a
Beamline	SPring8 BL44XU	SPring8 BL44XU
Wavelength (Å)	0.9000	0.9790
Oscillation range (º)	180	1080
Space group	C 2	C 2
Cell parameters (Å)	a = 180.2, b = 52.9, c = 78.4	a = 181.6, b = 53.5, c = 79.0
Resolution range (Å)	50.0 – 1.90 (1.94 – 1.90)	50.0 – 2.30 (2.34 – 2.30)
Observed reflections	215,719	702,336
Unique reflections	58,464	32,931
Completeness (%)	99.5 (99.3)	99.8 (99.2)
R _merge(I)^b	0.071 (0.586)	0.175 (> 1)
I / σ(I)	25.0 (2.5)	16.3 (3.6)
Refinement statistics
Resolution range (Å)	50.0 – 1.90
No. of protein atoms	5,644
No. of water molecules	553
R _work/R _free ^c	0.164/0.202 (0.244/0.304)
Rmsd^d from ideality bond length (Å)	0.007
angles (º)	1.1
Ramachandran plot (%)^e
Favored region	98.3
Allowed region	1.7
Outlier region	0.0

^aValues in parentheses are for the highest resolution shell.
^b R _merge(I) = (ΣΣ|I _i - < I > |)/ΣΣI _i, where I _i is the intensity of the i th observation and < I > is the mean intensity.
^c R _work/R _free = ∑|F _O - F _C|/∑|F _O|. R _work was calculated from the working set (95% of the total reflections). R _free was calculated from the test set, using 5% of the total reflections. The test set was not used in refinement.
^drmsd, root mean square deviation.
^eCalculated using the program RAMPAGE.